Arsenic in PDB 3hbz: Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution

The structure of Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution, PDB code: 3hbz was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.75 / 2.05
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.551, 94.551, 107.812, 90.00, 90.00, 120.00
R / Rfree (%)	15.9 / 19.1

The structure of Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Sodium	(Na)	2 atoms

The binding sites of Arsenic atom in the Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution (pdb code 3hbz). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution, PDB code: 3hbz:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:As5 b:50.4 occ:0.80 AS A:CAC5 0.0 50.4 0.8 O2 A:CAC5 1.7 50.8 0.8 O1 A:CAC5 1.7 44.0 0.8 C1 A:CAC5 1.9 43.0 0.8 C2 A:CAC5 2.0 40.8 0.8 CA A:CA2 3.5 51.2 0.8 O A:HOH586 3.5 38.9 1.0 O A:PHE101 3.7 24.1 1.0 N A:LYS103 4.0 24.4 1.0 CA A:TRP102 4.5 21.6 1.0 O A:LYS103 4.5 30.4 1.0 CE3 A:TRP102 4.6 27.8 1.0 C A:PHE101 4.7 23.0 1.0 C A:TRP102 4.8 23.3 1.0 CB A:LYS103 4.8 26.8 1.0 CA A:LYS103 4.9 26.3 1.0

Arsenic binding site 2 out of 2 in the Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of A Putative Glycoside Hydrolase (BT_2081) From Bacteroides Thetaiotaomicron Vpi-5482 at 2.05 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:As6 b:54.0 occ:0.60 AS A:CAC6 0.0 54.0 0.6 O1 A:CAC6 1.7 36.6 0.6 O2 A:CAC6 1.8 53.6 0.6 C1 A:CAC6 2.0 49.1 0.6 C2 A:CAC6 2.0 40.5 0.6 O A:HOH508 3.7 38.0 1.0 OG1 A:THR48 3.9 29.3 1.0 O A:HOH565 4.0 54.1 1.0 CB A:ASN49 4.0 30.8 1.0 OE1 A:GLN128 4.0 53.6 1.0 N A:ASN50 4.1 25.9 1.0 OD1 A:ASN50 4.2 46.7 1.0 N A:ASN49 4.2 27.0 1.0 CB A:THR48 4.3 26.3 1.0 CA A:ASN49 4.5 29.4 1.0 CB A:ASN50 4.6 27.1 1.0 O A:HOH493 4.6 42.3 1.0 C A:ASN49 4.7 28.9 1.0 CG A:ASN50 4.9 43.3 1.0 CA A:ASN50 4.9 28.6 1.0 CD A:GLN128 4.9 45.2 1.0 O A:HOH487 4.9 27.3 1.0 NE2 A:GLN128 5.0 36.9 1.0 OH A:TYR130 5.0 25.2 1.0

A.P.Yeh, P.Abdubek, T.Astakhova, H.L.Axelrod, C.Bakolitsa, X.Cai, D.Carlton, C.Chen, H.J.Chiu, M.Chiu, T.Clayton, D.Das, M.C.Deller, L.Duan, K.Ellrott, C.L.Farr, J.Feuerhelm, J.C.Grant, A.Grzechnik, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, P.Kozbial, S.S.Krishna, A.Kumar, W.W.Lam, D.Marciano, D.Mcmullan, M.D.Miller, A.T.Morse, E.Nigoghossian, A.Nopakun, L.Okach, C.Puckett, R.Reyes, H.J.Tien, C.B.Trame, H.Van Den Bedem, D.Weekes, T.Wooten, Q.Xu, K.O.Hodgson, J.Wooley, M.A.Elsliger, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson. Structure of Bacteroides Thetaiotaomicron BT2081 at 2.05 A Resolution: the First Structural Representative of A New Protein Family That May Play A Role in Carbohydrate Metabolism. Acta Crystallogr.,Sect.F V. 66 1287 2010.
ISSN: ESSN 1744-3091
PubMed: 20944224
DOI: 10.1107/S1744309110028228